ID A0A2K1IIR4_PHYPA Unreviewed; 1169 AA.
AC A0A2K1IIR4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Alpha-mannosidase {ECO:0000256|RuleBase:RU361199};
DE EC=3.2.1.- {ECO:0000256|RuleBase:RU361199};
GN ORFNames=PHYPA_027856 {ECO:0000313|EMBL:PNR29164.1};
OS Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR29164.1};
RN [1] {ECO:0000313|EMBL:PNR29164.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_10010V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=18079367; DOI=10.1126/science.1150646;
RA Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA Boore J.L.;
RT "The Physcomitrella genome reveals evolutionary insights into the conquest
RT of land by plants.";
RL Science 319:64-69(2008).
RN [2] {ECO:0000313|EMBL:PNR29164.1, ECO:0000313|Proteomes:UP000006727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c23_10010V3.1,
RC ECO:0000313|Proteomes:UP000006727};
RX PubMed=29237241; DOI=10.1111/tpj.13801;
RA Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA Schmutz J., Rensing S.A.;
RT "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT structure and evolution.";
RL Plant J. 93:515-533(2018).
RN [3] {ECO:0000313|EnsemblPlants:Pp3c23_10010V3.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (DEC-2020) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|RuleBase:RU361199};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU361199};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC {ECO:0000256|ARBA:ARBA00009792, ECO:0000256|RuleBase:RU361199}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABEU02000023; PNR29164.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K1IIR4; -.
DR STRING; 3218.A0A2K1IIR4; -.
DR PaxDb; 3218-PP1S10_34V6-1; -.
DR EnsemblPlants; Pp3c23_10010V3.1; Pp3c23_10010V3.1; Pp3c23_10010.
DR EnsemblPlants; Pp3c23_10010V3.2; Pp3c23_10010V3.2; Pp3c23_10010.
DR EnsemblPlants; Pp3c23_10010V3.3; Pp3c23_10010V3.3; Pp3c23_10010.
DR Gramene; Pp3c23_10010V3.1; Pp3c23_10010V3.1; Pp3c23_10010.
DR Gramene; Pp3c23_10010V3.2; Pp3c23_10010V3.2; Pp3c23_10010.
DR Gramene; Pp3c23_10010V3.3; Pp3c23_10010V3.3; Pp3c23_10010.
DR InParanoid; A0A2K1IIR4; -.
DR OrthoDB; 5474711at2759; -.
DR Proteomes; UP000006727; Chromosome 23.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042538; P:hyperosmotic salinity response; IEA:EnsemblPlants.
DR GO; GO:0006013; P:mannose metabolic process; IEA:InterPro.
DR GO; GO:0006491; P:N-glycan processing; IBA:GO_Central.
DR GO; GO:0006487; P:protein N-linked glycosylation; IEA:EnsemblPlants.
DR CDD; cd10809; GH38N_AMII_GMII_SfManIII_like; 1.
DR Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR011682; Glyco_hydro_38_C.
DR InterPro; IPR015341; Glyco_hydro_38_cen.
DR InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR InterPro; IPR000602; Glyco_hydro_38_N.
DR InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR InterPro; IPR013780; Glyco_hydro_b.
DR PANTHER; PTHR11607; ALPHA-MANNOSIDASE; 1.
DR PANTHER; PTHR11607:SF3; LYSOSOMAL ALPHA-MANNOSIDASE; 1.
DR Pfam; PF09261; Alpha-mann_mid; 1.
DR Pfam; PF07748; Glyco_hydro_38C; 1.
DR Pfam; PF01074; Glyco_hydro_38N; 1.
DR SMART; SM00872; Alpha-mann_mid; 1.
DR SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361199};
KW Hydrolase {ECO:0000256|RuleBase:RU361199};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361199};
KW Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU361199}.
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 494..575
FT /note="Glycoside hydrolase family 38 central"
FT /evidence="ECO:0000259|SMART:SM00872"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1169 AA; 132429 MW; D54A1BFD14398FF2 CRC64;
MAGGYGRSLP TYSSSLPGSN RKGSKRRSAG KSPPMFSWSW FVRPRTYLTL ASVVFTFLFL
FQGGFIVTSI SKATRKNPGQ NLSSILESQL RKKVFEGKRN GSSAHVGEAV VDITMKALYD
RIAFDDRDGG AWKQGWDVRY DGPEWDEEKL KVFVVPHSHN DPGWIRTVEE YYQERTRHIL
DTVVASLLKD PRRKFIWEEM SYLERWWRDA TPQSKEDLKR LVKSGQLEIV GGGWVMNDEA
NSHYFAIIEQ MTAGNLWLLD NVGVAPKNSW AIDPFGHSPT MAYLLRRMGF HNMLIQRTHY
EVKKELAWNK NLEFNWRQSW DFDNSTDIFC HMMPFYSYDI PHTCGPEPGV CCQFDYWRSP
GRAGYCPWNK QPQTITDENV KERAELLLDQ YRKKSVLYRS NTLLVPLGDD FRYIEMAEAD
LAYENYQKIF DYVNSHPNLK AELKFGTLED YFSTLRQEAT KKTTTKEFSN SPLSVPGFPS
LAGDFFTYAD IHQDYWSGYY VTRPFYKAVD RVLEQTLRAA DTLFMLARAF HGNEIATLSG
DVLERQRRNL ALFQHHDGVT GTAKDHVVVD YANKMHDGIV ELESLMAASV GEILGQKVRS
TPHLFESVEL RKSYDMLPVS KVVEIKNFKV QRVVFYNPLE ETLQQVAMVM VDNPAVCVFD
SLGKPVQSQL SPDWGAGITA SFTSKNHRLH FPVTVSPLGL ATYLITADTD NCDTASLSSV
SVFNEPRDFM CPDPYLCTYH PGGHERVSIS SSQQSLVFST QTGLLMSHKS SNGNELPVEE
EIAMYTSQGS GAYLFRPQGE AAPLVQSGGL VLVSKGPLVE EVHSVPKFNT LAPLVRSARL
YAGKTIQAAS AEFEYYVDFA RNEFNDRELI TRFKTDLNNK RIFYTDLNGF QTMRRETYSK
IPLQGNYYPM PSLAFLQCPG GRRFSIHSRQ ALGVASLHKG ELEIMLDRRL IHDDSRGLGQ
GIMDNRPSRV VFQLLVERNT SFSSPASDFH SKVPSLLSHL VNDQLNYPAH LFFDTPQPFT
SIQATTLNND MDTSFAPLRN SLPCDLHIVA MKTLRPSQAS PGEDYTHGVL FHRRGVDSSY
PMSDSITCST MEKQGFDVFT LFSPQIDITK LRKSSLSFVH TDGREVTLQK DAAHRKLGLG
GAFVGRSEGL LDLSPMELQA FKFKIKSVG
//
